title: Evidence for involvement of 2 histidine residues in the reaction of ampicillin acylase.
abstract: The chemical modification of purified ampicillin acylase by N-bromosuccinimide and diethylpyrocarbonate resulted in time-dependent inactivation of the enzyme. Both substrates, ampicillin and 6-aminopenicillanic acid, protected the enzyme against inactivation, suggesting that the modification occurred near or at the active site. Amino acid analyses and other data indicated that two histidyl residues per subunit molecule were essential for catalytic activity.
authors.affiliation: Department of Biological Science and Engineering, Korea Advanced Institute of Science and Technology, Seoul.
authors.forename: D J
authors.initials: DJ
authors.lastname: Kim
authors.forename: S M
authors.initials: SM
authors.lastname: Byun
mesh_terms: D000581:Amidohydrolases / Q000378:metabolism*; D001974:Bromosuccinimide / Q000494:pharmacology; D004047:Diethyl Pyrocarbonate / Q000494:pharmacology; D006639:Histidine / Q000378:metabolism; D010399:Penicillin Amidase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D011549:Pseudomonas / Q000201:enzymology*; D013329:Structure-Activity Relationship
chemical_list: D006639:Histidine; D000581:Amidohydrolases; C049057:ampicillin acylase; D010399:Penicillin Amidase; D001974:Bromosuccinimide; D004047:Diethyl Pyrocarbonate